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  (BBSRC DTP) Precision mapping of protein-protein interactions in living cells using radical trapping technology


   Department of Chemistry

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  Prof I Larrosa, Dr C.K Schmidt, Prof P Barran  No more applications being accepted  Competition Funded PhD Project (Students Worldwide)

About the Project

Intracellular signalling pathways rely on defined protein-protein interactions occurring in an ordered fashion at precise locations and times within the cell. Elucidation of such protein-protein interactions with high spatiotemporal resolution is therefore key for properly understanding cellular signalling events and developing therapies to treat the plethora of diseases caused by cell signalling alterations.

In this project we aim at developing a series of chemical and genetic engineering tools to allow the precise mapping of protein-protein interactions in intracellular systems. These tools will then, in the first instance, be applied to mapping DNA Damage Response (DDR) pathways. The DDR plays a major role in preventing prevalent diseases such as cancer, and promoting healthy ageing.

Moreover, the developed platform can be applied to almost any other question in cell biology to increase our fundamental understanding of the underlying signalling pathways and their associated disease pathologies.

·      https://personalpages.manchester.ac.uk/staff/igor.larrosa/research.html

·      https://www.research.manchester.ac.uk/portal/christine.schmidt.html

·      https://www.mbc.manchester.ac.uk/barrangroup/

Applicants must have obtained or be about to obtain a First or Upper Second class UK honours degree, or the equivalent qualifications gained outside the UK, in an appropriate area of science, engineering or technology.

Applicants interested in this project should make direct contact with the Primary Supervisor to arrange to discuss the project further as soon as possible.

How To Apply

To be considered for this project you MUST submit a formal online application form - full details on how to apply can be found on the BBSRC DTP website www.manchester.ac.uk/bbsrcdtpstudentships    

Equality, Diversity and Inclusion

Equality, diversity and inclusion is fundamental to the success of The University of Manchester, and is at the heart of all of our activities. The full Equality, diversity and inclusion statement can be found on the website https://www.bmh.manchester.ac.uk/study/research/apply/equality-diversity-inclusion/

Biological Sciences (4) Chemistry (6)

Funding Notes

Funding will cover tuition fees and stipend only. This scheme is open to both UK and international applicants. However, we are only able to offer a limited number of studentships to applicants outside the UK. Therefore, full studentships will only be awarded to exceptional quality candidates, due to the competitive nature of this scheme.

References

1) Matthew Wheatley, Michael Findlay, Rocio Lopez-Rodriguez, Diego M. Cannas, Marco Simonetti, Larrosa, I.* (2021). Ru-catalyzed room-temperature alkylation and late-stage alkylation of arenes with primary alkyl bromides. Chem Catal., 1, in press.
• New chemistry journal from Cell Press.
2) Gang-Wei Wang, Matthew Wheatley, Marco Simonetti, Diego M. Cannas, Larrosa, I.* (2020). Cyclometalated Ruthenium Catalyst Enables Ortho-Selective C–H Alkylation with Secondary Alkyl Bromides. Chem., 6, 1459.
• IF 23, ranked 1st for original research in Chemistry.
3) Simonetti, M., Cannas, D. M., Just-Baringo, X., Vitorica-Yrezabal, I., Larrosa, I.* (2018). A Cyclometalated Ruthenium-catalyst enables late stage functionalisation of pharmaceuticals. Nat. Chem., 724‒731.
• IF 22, ranked 2nd for original research in Chemistry.
4) Cabello-Lobato, M.J., Jenner, M., Loch, C.M., Jackson, S.P., Wu, Q., Cliff, M.J., and Schmidt, C.K.* (2021). Microarray screening reveals a non-conventional SUMO-binding mode linked to DNA repair by non-homologous end-joining. BioRxiv ID: 10.1101/2021.01.20.427433.
5) Beveridge R, Migas LG, Das RK, Pappu R V., Kriwacki RW, Barran PE*. Ion Mobility Mass Spectrometry Uncovers the Impact of the Patterning of Oppositely Charged Residues on the Conformational Distributions of Intrinsically Disordered Proteins. J Am Chem Soc. 2019;141(12):4908-4918. doi:10.1021/jacs.8b13483
• IF 15, ranked 3rd for original research in Chemistry.

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